Rabbit anti-Human ICAM-1 mAb(CAP) (RM18057)

Intercellular Adhesion Molecule 1 (ICAM-1), also known as CD54, is a nearly ubiquitous transmembrane glycoprotein that plays a key role in leukocyte migration and activation . Human ICAM-1 contains five Ig-like domains in its extracellular domain (ECD) and associates into non-covalently linked dimers. Soluble forms of monomeric and dimeric ICAM-1 (sICAM-1) can be generated via proteolytic cleavage by cathepsin G, elastase, MMP-9, MMP-14/MT1-MMP, and TACE/ADAM17. In the mouse, alternate splicing generates isoforms that lack particular Ig-like domains and are differentially sensitive to proteolysis. Within the ECD, human ICAM-1 shares 53% amino acid sequence identity with mouse and rat ICAM-1.The principal binding partners of ICAM-1 are the leukocyte integrins LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18). The multivalency of dimeric ICAM-1 increases its strength of interaction with LFA-1. ICAM-1 also binds several non-integrin ligands includingCD43/sialophorin, fibrinogen, hyaluronan, rhinoviruses, and Plasmodium falciparum-infected erythrocytes. At sites of inflammation, ICAM-1 is upregulated on endothelial and epithelial cells where it mediates the adhesion and paracellular migration of leukocytes expressing activated LFA-1 and Mac-1.ICAM-1 ligation prolongs antigen presentation by dendritic cells and promotes T cell proliferation and cytokine release .ICAM-1 activation also participates in angiogenesis, wound healing, and bone metabolism.